This document summarizes various metal ion transport and storage systems in the body. It discusses ionophores, which are molecules that transport metal ions across membranes. It also describes ferritin, which stores iron in a non-toxic form in tissues, and transferrin, a protein carrier that transports iron throughout the body. Additionally, it outlines metallothioneins, cysteine-rich proteins that bind metals to protect cells from toxicity. Finally, it mentions some medicinal applications of metal-containing compounds like cisplatin, which is used as a chemotherapy drug.
Disentangling the origin of chemical differences using GHOST
Metal ion transport & storage: Ionophores, ferritin, transferrin & medicinal applications
1.
2. METAL ION TRANSPORT &
STORAGE:
IONOPHORES , FERRITIN ,
TRANS-FERRIN ,
METALLOTHIONINS &
MEDICINAL APPLICATIONS OF
Cis-platin & RELATED COMPOUNDS.
3. IONOPHORES:
IT IS A CHEMICAL SPECIES WHICH BINDS METAL ION TO TRANSPORT THEM
ACROSS BIOLOGICAL MEMBRANES .
IONOPHORE MEANS ION CARRIER .
These compounds catalyze ion transport across hydrophobic membranes such as
liquid polymeric membranes (carrier-based ion selective electrodes) or lipid bilayers
found in the living cells or synthetic vesicles .
4. FUNCTION OF IONOPHORES :
• Ionophores increase permeability in lipid
bilayer membranes by two different
mechanisms.
• They transport metal ions like Na+ , k+
which are lipophilic (lipid binder) , as
movement of this metal require special
carrier mechanism .
5. EXAMPLE OF IONOPHORES :
THERE ARE MANY EXAMPLE OF IONOPHORES USED BASICALLY FOR
ANTIBIOTICS , MAINTAINING OSMOTIC BALANCE , HORMONE ACTION ,
NEUROTRANSMISSION ETC .
1) VALINOMYCIN – MADE UP OF VALINE ,ETC IT IS A K+ CARRIER , 6 OXYGEN OF
IONOPHORE INTERACT WITH K+ BOUNDED .
6. FERRITIN :
FERRITIN IS A PROTIEN IN WHICH Fe IS STORED IN
NON-TOXIC FORM .
IT IS PRESENT IN SPLEEN , BONE MARROW & LIVER
.
IT IS FORMED BY BIOMINERALIZATION PROCESS .
THIS BIO MINERAL IS INSOLUBLE BUT SOLUBLE IN
BIOLOGICAL FLUIDS .
7. CHEMICAL WORKING OF FERRITIN :
IT CONSISTS OF 3 PARTS : PROTIEN COAT , IRON
PROTIEN INTERFACE & ION CORE .
ION (Fe+3) IS DEPOSITED IN OXIDIZED FORM
Fe2O3(H2O) WITH VARIOUS AMOUNT OF PHOSPHATE .
Fe+3 OXIDIZES & SURROUNDED OCTAHEDRALLY BY
OXYGEN .
Fe+3 IS HIGH SPIN COMPLEX WHICH UNDERGOES
STRONG ANTI-FERROMAGNETIC COUPLING .
……TO BE CONTD
8. THE OH- & PO4-3 HELP TO BALANCE THE
CHARGE & BINDING AT PROTIEN SURFACE .
PROTIEN SHEATH CONSISTS OF 24 SUB-UNITS
OF COILED POLYPEPTIDE …THERE ARE TWO
ENDS N-POLAR TERMINAL & E-NONPOLAR
TERMINAL .
9.
10. TRANSFERRIN :
• TRANSFERRIN ACTS AS A CARRIER OF IRON .
• Transferrin are iron-binding blood plasma glycoproteins that control the level of
free iron in biological fluids & TRANSPORT IRON THROUGHOUT THE BODY .
• IT MAINLY TRANSPORT Fe FROM RBC’S BREAKDOWN SITE TO PLACE OF BIO-
SYNTHESIS OF RBC .
• EG: LACTOFERRIN IN MILK ,CONALBUMIN IN EGG-WHITE & SERUM
TRANSFERRIN IN BLOOD .
11. CHEMICAL WORKING OF TRANSFERRIN :
• EACH Fe US SURROUNDED BY 5 BINDING SITE COMING
FROM PROTIEN CHAIN .
• 1 NITROGEN FROM IMIDZOLE GROUP OF HISIDINE , 2
PHENOLIC OXYGEN FROM TYROSINE , ONE OXYGEN OF
ASPARTATE & ANION OF CO3 -2 OR HCO3- TOGETHER
FORM OCTAHEDRAL CHELATE .
• WITHOUT HCO3 OR CO3 CHELATE RING DESTABILIZES .
• AT PH 7 FE+3 IS VERY STABLE BUT AT SLGHTLY LOW PH
THE Fe DISSOCIATES FROM CHELATE .
12.
13. METALLOTHIONINS :
• Metallothioneins (MTs) are a family of small, highly
conserved, cysteine-rich metal-binding proteins that
are important for zinc and copper homeostasis,
protection against oxidative stress, and buffering
against toxic heavy metals.
• It protects cells from metal toxicity by binding metal
ions. Metallothioneins may also be important for
intestinal and renal absorption of metals and for
metal storage and excretion.
• It occurs in liver , kidney & spleen .
14. CHEMICALLY WORKING OF
METALLOTHIONINES :
IT COMPOSED OF 61-62 AMINO ACID RESIDUE .
DUE TO HIGH % OF THIOL GROUP BEARING AMINO ACIDS
STABILITY CONSTANT WITH METAL IONS .(LEWIS ACID).
TO STOP DENATURE OF ENZYME PROTIEN BY ATTACK OF
HEAVY METAL , NATURE HAS DESIGNED SERIES OF THIOL GRP
CONTAINING PROTIENS THIONEINS .
THE C TERMINAL IS 𝛼 DOMAIN HAS WITH 11 CYSTIENS & N
TERMINAL HAS ß DOMAIN WITH 9 CYSTIENES .
MOLECULAR WIEGHT 500-14000 Da .